BMCB-Faculty Research, Darrel E. Goll

Professor of Nutritional Sciences and Biochemistry & Molecular Biophysics
Ph.D., University of Wisconsin

Role of contractile proteins and the Ca2+ dependent proteinase in cell function.

Research Interests

Proteins similar to the contractile proteins of muscle are found in all eucaryotic cells. Their roles in non-muscle cells include: cell migration, cell ruffling, and cytokinesis. The major contractile protein is actin and the interaction of actin with its binding proteins is critical to the various cytoskeletal structures in the cell. One example is dystrophin. (Dystrophin is a critical actin-binding protein missing in several muscular dystrophies.) We are interested in the involvement of several actin-binding proteins (e.g. alpha-actinin, vinculin and tropomyosin) and their effects on cytoskeletal structure. We are also studying the roles of Ca2+-dependent proteinases (u-calpain and m-calpain) and their inhibitor (calpastatin) in turnover of cytoskeletal proteins. The calpains exist in most cells and may be specific for degrading actin-binding proteins, particularly those at the membrane. We are studying the different domains of the calpains and an important objective is to identify regulatory mechanisms, and recent evidence indicates that phosphorylation of calpain may be important.

Select Publications

Any link on the below references will take you off of the BMCB site and to an abstract of that particular paper.

Zalewska, T., V.F. Thompson, and D.E. Goll. 2004. Effect of phosphatidylinositol and inside-out erythrocyte vesicles on autolysis of mu- and m-calpain from bovine skeletal muscle. Biochimica et Biophysica Acta 1693: 125-133.

Wendt, A., V.F. Thompson, and D.E. Goll. 2004. Interaction of calpastatin with calpain: a review. Biological Chemistry 385: 465-472.

Li, H., V.F. Thompson, and D.E. Goll. 2004. Effects of autolysis on properties of mu- and m-calpain. Biochimica et Biophysica Acta 1691: 91-103.

Goll, D.E., V.F. Thompson, H. Li, W. Wei, and J. Cong. 2003. The calpain system. Physiological Reviews 83: 731-801.

Thompson, V.F., K.R. Lawson, J. Barlow, and D.E. Goll. 2003. Digestion of mu- and m-calpain by trypsin and chymotrypsin. Biochimica et Biophysica Acta 1648: 140-153.

Thompson, V.F., S. Saldana, J. Cong, D.M. Luedke, and D.E. Goll. 2002. The calpain system in human placenta. Life Sciences 70: 2493-2508.

Cong, J., V.F. Thompson, and D.E. Goll. 2002. Immunoaffinity purification of the calpains. Protein Expression and Purification 25: 283-290.

Wei, W., H. Li, J. Cong, V.P. Thompson, and D.E. Goll. 2002. Immunoaffinity purification of calpastatin and calpastatin constructs. Biochimica et Biophysica Acta 1597: 97-106.

Kulkarni. S., D.e. Goll, J.E. Fox. 2002. Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly and cell spreading. Journal of Biological Chemistry 277: 24435-24441.

Delgado, E.F., G.H. Geesink, J.A. Marchello, D.E. Goll, and M. Koohmaraie. 2001. Properties of myofibril-bound calpain activity in longissimus muscle of callipyge and normal sheep. Journal of Animal Science 79: 2097-2107.

Cottin, P., V.F. Thompson, S.K. Sathe, A. Szpacenko, and D.E. Goll. 2001. Autolysis of mu- and m-calpain from bovine skeletal muscle. Biological Chemistry 382: 767-776.

Delgado, E.F., G.H. Geesink, J.A. Marchello, D.E. Goll, and M. Koohmaraie. 2001. The calpain system in three muscles of normal and callipyge sheep. Journal of Animal Science 79: 398-412.

Bialkowska, K., S. Kulkarni, X. Du, D.E. Goll, T.C. Saido, and J.E. Fox. 2000. Evidence that beta3 integrin-induced Rac activation involves the calpain-dependent formation of integrin clusters that are distinct from the focal complexes and focal adhesions that form as Rac and RhoA become active. Journal of Cell Biology 151: 685-696.

Thompson, V.F., and D.E. Goll. 2000. Purification of mu-calpain, m-calpain, and calpastatin from animal tissues. Methods in Molecular Biology 144: 3-16.

Thompson, V.F., S. Saldana, J. Cong, and D.E. Goll. 2000. A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteases. Analytical Biochemistry 279: 170-178.

Thompson, V.F., K. Lawson, and D.E. Goll. 2000. Effect of mu-calpain on m-calpain. Biochemical and Biophysical Research Communications 267: 495-499.

Contact Information

Mailing:
Darrel E. Goll, Professor
Department of Nutritional Sciences
University of Arizona
Shantz 642
P.O. Box 210038
Tucson, AZ 85721-0038

Web Site: Home Page

Telephone:
520-621-7236 (Office)
520-621-7790 (Lab)

Fax:
520-621-1396

Email:
darrelg@ag.arizona.edu

Please e-mail any comments to:
bmcb@email.arizona.edu